ID NEK1_HUMAN Reviewed; 1258 AA. AC Q96PY6; G5E9Z3; Q05DG5; Q14CB7; Q5H9T1; Q6PIB8; Q96SS2; Q9H6P7; Q9Y594; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-2002, sequence version 2. DT 27-MAR-2024, entry version 204. DE RecName: Full=Serine/threonine-protein kinase Nek1; DE EC=2.7.11.1 {ECO:0000269|PubMed:20230784}; DE AltName: Full=Never in mitosis A-related kinase 1; DE Short=NimA-related protein kinase 1; DE AltName: Full=Renal carcinoma antigen NY-REN-55; GN Name=NEK1; Synonyms=KIAA1901; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11572484; DOI=10.1093/dnares/8.4.179; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXI. The RT complete sequences of 60 new cDNA clones from brain which code for large RT proteins."; RL DNA Res. 8:179-187(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-724. RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Bone marrow, and Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-1258 (ISOFORM 5), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 865-1258. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 444-1258 (ISOFORM 2), AND IDENTIFICATION AS A RP RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [8] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15604234; DOI=10.1158/0008-5472.can-04-2243; RA Polci R., Peng A., Chen P.L., Riley D.J., Chen Y.; RT "NIMA-related protein kinase 1 is involved early in the ionizing radiation- RT induced DNA damage response."; RL Cancer Res. 64:8800-8803(2004). RN [9] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=18843199; DOI=10.4161/cc.7.20.6815; RA Chen Y., Chen P.L., Chen C.F., Jiang X., Riley D.J.; RT "Never-in-mitosis related kinase 1 functions in DNA damage response and RT checkpoint control."; RL Cell Cycle 7:3194-3201(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414; SER-418; SER-428; RP SER-653; SER-798; SER-834; SER-868 AND SER-881, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP FUNCTION IN PHOSPHORYLATION OF VDAC1, AND CATALYTIC ACTIVITY. RX PubMed=20230784; DOI=10.1016/j.bbrc.2010.03.077; RA Chen Y., Gaczynska M., Osmulski P., Polci R., Riley D.J.; RT "Phosphorylation by Nek1 regulates opening and closing of voltage dependent RT anion channel 1."; RL Biochem. Biophys. Res. Commun. 394:798-803(2010). RN [14] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN RP DIGENIC SHORT-RIB THORACIC DYSPLASIA 3/6 WITH POLYDACTYLY. RX PubMed=21211617; DOI=10.1016/j.ajhg.2010.12.004; RA Thiel C., Kessler K., Giessl A., Dimmler A., Shalev S.A., von der Haar S., RA Zenker M., Zahnleiter D., Stoess H., Beinder E., Abou Jamra R., Ekici A.B., RA Schroeder-Kress N., Aigner T., Kirchner T., Reis A., Brandstaetter J.H., RA Rauch A.; RT "NEK1 mutations cause short-rib polydactyly syndrome type majewski."; RL Am. J. Hum. Genet. 88:106-114(2011). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-428; THR-661; RP SER-664; SER-868; SER-881 AND SER-1052, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH RP CFAP410 AND SPATA7 BY MASS SPECTROMETRY, AND INTERACTION WITH CFAP410. RX PubMed=26167768; DOI=10.1038/ncb3201; RG UK10K Consortium; RG University of Washington Center for Mendelian Genomics; RA Wheway G., Schmidts M., Mans D.A., Szymanska K., Nguyen T.M., Racher H., RA Phelps I.G., Toedt G., Kennedy J., Wunderlich K.A., Sorusch N., RA Abdelhamed Z.A., Natarajan S., Herridge W., van Reeuwijk J., Horn N., RA Boldt K., Parry D.A., Letteboer S.J., Roosing S., Adams M., Bell S.M., RA Bond J., Higgins J., Morrison E.E., Tomlinson D.C., Slaats G.G., RA van Dam T.J., Huang L., Kessler K., Giessl A., Logan C.V., Boyle E.A., RA Shendure J., Anazi S., Aldahmesh M., Al Hazzaa S., Hegele R.A., Ober C., RA Frosk P., Mhanni A.A., Chodirker B.N., Chudley A.E., Lamont R., RA Bernier F.P., Beaulieu C.L., Gordon P., Pon R.T., Donahue C., RA Barkovich A.J., Wolf L., Toomes C., Thiel C.T., Boycott K.M., McKibbin M., RA Inglehearn C.F., Stewart F., Omran H., Huynen M.A., Sergouniotis P.I., RA Alkuraya F.S., Parboosingh J.S., Innes A.M., Willoughby C.E., Giles R.H., RA Webster A.R., Ueffing M., Blacque O., Gleeson J.G., Wolfrum U., RA Beales P.L., Gibson T., Doherty D., Mitchison H.M., Roepman R., RA Johnson C.A.; RT "An siRNA-based functional genomics screen for the identification of RT regulators of ciliogenesis and ciliopathy genes."; RL Nat. Cell Biol. 17:1074-1087(2015). RN [19] RP VARIANTS [LARGE SCALE ANALYSIS] PHE-10; LYS-25; VAL-76; PRO-294; GLY-355; RP VAL-463; THR-598; GLY-724; ASN-745; GLU-883 AND ASN-1180. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [20] RP VARIANTS SRTD6 ARG-145 AND SER-253. RX PubMed=22499340; DOI=10.1136/jmedgenet-2011-100717; RA El Hokayem J., Huber C., Couve A., Aziza J., Baujat G., Bouvier R., RA Cavalcanti D.P., Collins F.A., Cordier M.P., Delezoide A.L., Gonzales M., RA Johnson D., Le Merrer M., Levy-Mozziconacci A., Loget P., RA Martin-Coignard D., Martinovic J., Mortier G.R., Perez M.J., Roume J., RA Scarano G., Munnich A., Cormier-Daire V.; RT "NEK1 and DYNC2H1 are both involved in short rib polydactyly Majewski type RT but not in Beemer Langer cases."; RL J. Med. Genet. 49:227-233(2012). RN [21] RP INVOLVEMENT IN ALS24, AND VARIANTS 784-ARG--GLU-1258 DEL AND RP 1008-SER--GLU-1258 DEL. RX PubMed=26945885; DOI=10.1093/brain/aww033; RA Brenner D., Mueller K., Wieland T., Weydt P., Boehm S., Lule D., RA Huebers A., Neuwirth C., Weber M., Borck G., Wahlqvist M., Danzer K.M., RA Volk A.E., Meitinger T., Strom T.M., Otto M., Kassubek J., Ludolph A.C., RA Andersen P.M., Weishaupt J.H.; RT "NEK1 mutations in familial amyotrophic lateral sclerosis."; RL Brain 139:E28-E28(2016). RN [22] RP INVOLVEMENT IN ALS24, AND VARIANTS HIS-261 AND 550-ARG--GLU-1258 DEL. RX PubMed=27455347; DOI=10.1038/ng.3626; RA Kenna K.P., van Doormaal P.T., Dekker A.M., Ticozzi N., Kenna B.J., RA Diekstra F.P., van Rheenen W., van Eijk K.R., Jones A.R., Keagle P., RA Shatunov A., Sproviero W., Smith B.N., van Es M.A., Topp S.D., Kenna A., RA Miller J.W., Fallini C., Tiloca C., McLaughlin R.L., Vance C., Troakes C., RA Colombrita C., Mora G., Calvo A., Verde F., Al-Sarraj S., King A., RA Calini D., de Belleroche J., Baas F., van der Kooi A.J., de Visser M., RA Ten Asbroek A.L., Sapp P.C., McKenna-Yasek D., Polak M., Asress S., RA Munoz-Blanco J.L., Strom T.M., Meitinger T., Morrison K.E., Lauria G., RA Williams K.L., Leigh P.N., Nicholson G.A., Blair I.P., Leblond C.S., RA Dion P.A., Rouleau G.A., Pall H., Shaw P.J., Turner M.R., Talbot K., RA Taroni F., Boylan K.B., Van Blitterswijk M., Rademakers R., RA Esteban-Perez J., Garcia-Redondo A., Van Damme P., Robberecht W., Chio A., RA Gellera C., Drepper C., Sendtner M., Ratti A., Glass J.D., Mora J.S., RA Basak N.A., Hardiman O., Ludolph A.C., Andersen P.M., Weishaupt J.H., RA Brown R.H. Jr., Al-Chalabi A., Silani V., Shaw C.E., van den Berg L.H., RA Veldink J.H., Landers J.E.; RT "NEK1 variants confer susceptibility to amyotrophic lateral sclerosis."; RL Nat. Genet. 48:1037-1042(2016). CC -!- FUNCTION: Phosphorylates serines and threonines, but also appears to CC possess tyrosine kinase activity (PubMed:20230784). Involved in DNA CC damage checkpoint control and for proper DNA damage repair CC (PubMed:20230784). In response to injury that includes DNA damage, NEK1 CC phosphorylates VDAC1 to limit mitochondrial cell death CC (PubMed:20230784). May be implicated in the control of meiosis (By CC similarity). Involved in cilium assembly (PubMed:21211617). CC {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:20230784, CC ECO:0000269|PubMed:21211617}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:20230784}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20230784}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Binds to CBY2 (By similarity). Found in a complex with CC CFAP410, NEK1 and SPATA7 (PubMed:26167768). Interacts with CFAP410 CC (PubMed:26167768). Interacts (via Ser-1052 phosphorylated form) with CC 14-3-3 proteins (By similarity). {ECO:0000250|UniProtKB:P51954, CC ECO:0000269|PubMed:26167768}. CC -!- INTERACTION: CC Q96PY6; Q99689: FEZ1; NbExp=2; IntAct=EBI-373615, EBI-396435; CC Q96PY6; Q9UHY8: FEZ2; NbExp=2; IntAct=EBI-373615, EBI-396453; CC Q96PY6; Q5S007: LRRK2; NbExp=2; IntAct=EBI-373615, EBI-5323863; CC Q96PY6; Q04917: YWHAH; NbExp=4; IntAct=EBI-373615, EBI-306940; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15604234, CC ECO:0000305|PubMed:21211617}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P51954}. Cytoplasm CC {ECO:0000269|PubMed:18843199}. Note=Associated with the pericentriolar CC material (PubMed:21211617). Localizes to centrosome during interphase CC and mitosis (By similarity). Translocated from cytoplasm to discrete CC nuclear foci at sites of DNA damage (PubMed:15604234). CC {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:15604234, CC ECO:0000269|PubMed:21211617}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q96PY6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96PY6-2; Sequence=VSP_004870; CC Name=3; CC IsoId=Q96PY6-3; Sequence=VSP_035439; CC Name=4; CC IsoId=Q96PY6-4; Sequence=VSP_035435, VSP_035436; CC Name=5; CC IsoId=Q96PY6-5; Sequence=VSP_035437, VSP_035438; CC Name=6; CC IsoId=Q96PY6-6; Sequence=VSP_035436, VSP_035439; CC -!- TISSUE SPECIFICITY: High fetal expression in the brain and kidney. CC {ECO:0000269|PubMed:21211617}. CC -!- DISEASE: Short-rib thoracic dysplasia 6 with or without polydactyly CC (SRTD6) [MIM:263520]: A form of short-rib thoracic dysplasia, a group CC of autosomal recessive ciliopathies that are characterized by a CC constricted thoracic cage, short ribs, shortened tubular bones, and a CC 'trident' appearance of the acetabular roof. Polydactyly is variably CC present. Non-skeletal involvement can include cleft lip/palate as well CC as anomalies of major organs such as the brain, eye, heart, kidneys, CC liver, pancreas, intestines, and genitalia. Some forms of the disease CC are lethal in the neonatal period due to respiratory insufficiency CC secondary to a severely restricted thoracic cage, whereas others are CC compatible with life. Disease spectrum encompasses Ellis-van Creveld CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer- CC Saldino syndrome, and short rib-polydactyly syndrome. CC {ECO:0000269|PubMed:22499340}. Note=The disease is caused by variants CC affecting the gene represented in this entry. In some cases NEK1 CC mutations result in disease phenotype in the presence of mutations in CC DYNC2H1 indicating digenic inheritance (digenic short rib-polydactyly CC syndrome 3/6 with polydactyly) (PubMed:21211617). CC {ECO:0000269|PubMed:21211617}. CC -!- DISEASE: Amyotrophic lateral sclerosis 24 (ALS24) [MIM:617892]: A form CC of amyotrophic lateral sclerosis, a neurodegenerative disorder CC affecting upper motor neurons in the brain and lower motor neurons in CC the brain stem and spinal cord, resulting in fatal paralysis. Sensory CC abnormalities are absent. The pathologic hallmarks of the disease CC include pallor of the corticospinal tract due to loss of motor neurons, CC presence of ubiquitin-positive inclusions within surviving motor CC neurons, and deposition of pathologic aggregates. The etiology of CC amyotrophic lateral sclerosis is likely to be multifactorial, involving CC both genetic and environmental factors. The disease is inherited in 5- CC 10% of the cases. {ECO:0000269|PubMed:26945885, CC ECO:0000269|PubMed:27455347}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH15147.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAB15207.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB67794.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB067488; BAB67794.1; ALT_INIT; mRNA. DR EMBL; CR933642; CAI45943.1; -; mRNA. DR EMBL; AC116615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116621; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084724; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04791.1; -; Genomic_DNA. DR EMBL; BC015147; AAH15147.1; ALT_SEQ; mRNA. DR EMBL; BC037790; AAH37790.1; -; mRNA. DR EMBL; BC114491; AAI14492.1; -; mRNA. DR EMBL; AK025658; BAB15207.1; ALT_INIT; mRNA. DR EMBL; AK027580; BAB55209.1; ALT_INIT; mRNA. DR EMBL; AF155113; AAD42879.1; -; mRNA. DR CCDS; CCDS47162.1; -. [Q96PY6-1] DR CCDS; CCDS56348.1; -. [Q96PY6-4] DR CCDS; CCDS56349.1; -. [Q96PY6-2] DR CCDS; CCDS56350.1; -. [Q96PY6-6] DR CCDS; CCDS56351.1; -. [Q96PY6-3] DR RefSeq; NP_001186326.1; NM_001199397.1. [Q96PY6-3] DR RefSeq; NP_001186327.1; NM_001199398.1. [Q96PY6-6] DR RefSeq; NP_001186328.1; NM_001199399.1. [Q96PY6-4] DR RefSeq; NP_001186329.1; NM_001199400.1. [Q96PY6-2] DR RefSeq; NP_036356.1; NM_012224.2. [Q96PY6-1] DR RefSeq; XP_011530305.1; XM_011532003.1. DR RefSeq; XP_011530306.1; XM_011532004.1. [Q96PY6-2] DR PDB; 4APC; X-ray; 2.10 A; A/B=1-328. DR PDB; 4B9D; X-ray; 1.90 A; A/B=1-328. DR PDBsum; 4APC; -. DR PDBsum; 4B9D; -. DR AlphaFoldDB; Q96PY6; -. DR SMR; Q96PY6; -. DR BioGRID; 110825; 85. DR IntAct; Q96PY6; 46. DR MINT; Q96PY6; -. DR STRING; 9606.ENSP00000424757; -. DR BindingDB; Q96PY6; -. DR ChEMBL; CHEMBL5855; -. DR DrugBank; DB12010; Fostamatinib. DR GuidetoPHARMACOLOGY; 2114; -. DR iPTMnet; Q96PY6; -. DR PhosphoSitePlus; Q96PY6; -. DR BioMuta; NEK1; -. DR DMDM; 22256934; -. DR EPD; Q96PY6; -. DR jPOST; Q96PY6; -. DR MassIVE; Q96PY6; -. DR MaxQB; Q96PY6; -. DR PaxDb; 9606-ENSP00000424757; -. DR PeptideAtlas; Q96PY6; -. DR ProteomicsDB; 34091; -. DR ProteomicsDB; 77788; -. [Q96PY6-1] DR ProteomicsDB; 77789; -. [Q96PY6-2] DR ProteomicsDB; 77790; -. [Q96PY6-3] DR ProteomicsDB; 77791; -. [Q96PY6-4] DR ProteomicsDB; 77792; -. [Q96PY6-5] DR Pumba; Q96PY6; -. DR TopDownProteomics; Q96PY6-3; -. [Q96PY6-3] DR Antibodypedia; 28454; 180 antibodies from 27 providers. DR DNASU; 4750; -. DR Ensembl; ENST00000439128.6; ENSP00000408020.2; ENSG00000137601.18. [Q96PY6-1] DR Ensembl; ENST00000507142.6; ENSP00000424757.2; ENSG00000137601.18. [Q96PY6-3] DR Ensembl; ENST00000510533.5; ENSP00000427653.1; ENSG00000137601.18. [Q96PY6-2] DR Ensembl; ENST00000511633.5; ENSP00000423332.1; ENSG00000137601.18. [Q96PY6-6] DR Ensembl; ENST00000512193.5; ENSP00000424938.1; ENSG00000137601.18. [Q96PY6-4] DR GeneID; 4750; -. DR KEGG; hsa:4750; -. DR MANE-Select; ENST00000507142.6; ENSP00000424757.2; NM_001199397.3; NP_001186326.1. [Q96PY6-3] DR UCSC; uc003isb.3; human. [Q96PY6-1] DR AGR; HGNC:7744; -. DR CTD; 4750; -. DR DisGeNET; 4750; -. DR GeneCards; NEK1; -. DR HGNC; HGNC:7744; NEK1. DR HPA; ENSG00000137601; Low tissue specificity. DR MalaCards; NEK1; -. DR MIM; 263520; phenotype. DR MIM; 604588; gene. DR MIM; 617892; phenotype. DR neXtProt; NX_Q96PY6; -. DR OpenTargets; ENSG00000137601; -. DR Orphanet; 803; Amyotrophic lateral sclerosis. DR Orphanet; 2751; Orofaciodigital syndrome type 2. DR Orphanet; 93269; Short rib-polydactyly syndrome, Majewski type. DR PharmGKB; PA31545; -. DR VEuPathDB; HostDB:ENSG00000137601; -. DR eggNOG; KOG0589; Eukaryota. DR GeneTree; ENSGT00940000158460; -. DR HOGENOM; CLU_000288_60_1_1; -. DR InParanoid; Q96PY6; -. DR OMA; SATEXIS; -. DR OrthoDB; 198307at2759; -. DR PhylomeDB; Q96PY6; -. DR TreeFam; TF333575; -. DR PathwayCommons; Q96PY6; -. DR SignaLink; Q96PY6; -. DR SIGNOR; Q96PY6; -. DR BioGRID-ORCS; 4750; 51 hits in 1199 CRISPR screens. DR ChiTaRS; NEK1; human. DR GeneWiki; NEK1; -. DR GenomeRNAi; 4750; -. DR Pharos; Q96PY6; Tchem. DR PRO; PR:Q96PY6; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q96PY6; Protein. DR Bgee; ENSG00000137601; Expressed in secondary oocyte and 212 other cell types or tissues. DR ExpressionAtlas; Q96PY6; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IMP:CACAO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:CACAO. DR CDD; cd08218; STKc_Nek1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1. DR PANTHER; PTHR44899:SF4; SERINE_THREONINE-PROTEIN KINASE NEK1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q96PY6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amyotrophic lateral sclerosis; KW ATP-binding; Cell cycle; Cell division; Ciliopathy; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Kinase; Magnesium; KW Metal-binding; Mitosis; Neurodegeneration; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase; Tyrosine-protein kinase. FT CHAIN 1..1258 FT /note="Serine/threonine-protein kinase Nek1" FT /id="PRO_0000086418" FT DOMAIN 4..258 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 330..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..600 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 685..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1118..1171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 338..360 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 654..669 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 156 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 162 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:23186163" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51954" FT MOD_RES 653 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 661 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 664 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 798 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:23186163" FT MOD_RES 881 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1052 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1126 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51954" FT VAR_SEQ 398..422 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035435" FT VAR_SEQ 477..520 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035436" FT VAR_SEQ 478..521 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10508479" FT /id="VSP_004870" FT VAR_SEQ 522..527 FT /note="QKGQLA -> LDCDDP (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035437" FT VAR_SEQ 528..1258 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035438" FT VAR_SEQ 555 FT /note="M -> MGILQNLAAMYGGRPSSSRGGKPRNKEEE (in isoform 3 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_035439" FT VARIANT 10 FT /note="I -> F (in dbSNP:rs34214559)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040900" FT VARIANT 25 FT /note="E -> K (in a lung large cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040901" FT VARIANT 76 FT /note="L -> V (in dbSNP:rs35093214)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040902" FT VARIANT 145 FT /note="G -> R (in SRTD6; dbSNP:rs431905508)" FT /evidence="ECO:0000269|PubMed:22499340" FT /id="VAR_069617" FT VARIANT 253 FT /note="L -> S (in SRTD6)" FT /evidence="ECO:0000269|PubMed:22499340" FT /id="VAR_069618" FT VARIANT 261 FT /note="R -> H (risk factor for ALS24; dbSNP:rs200161705)" FT /evidence="ECO:0000269|PubMed:27455347" FT /id="VAR_080694" FT VARIANT 294 FT /note="A -> P (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040903" FT VARIANT 355 FT /note="R -> G (in dbSNP:rs35763578)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040904" FT VARIANT 463 FT /note="A -> V (in dbSNP:rs34540355)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040905" FT VARIANT 550..1258 FT /note="Missing (risk factor for ALS24)" FT /evidence="ECO:0000269|PubMed:27455347" FT /id="VAR_080695" FT VARIANT 598 FT /note="A -> T (in dbSNP:rs33933790)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_046486" FT VARIANT 717 FT /note="N -> K (in dbSNP:rs34324114)" FT /id="VAR_061743" FT VARIANT 724 FT /note="E -> G (in dbSNP:rs34099167)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:17974005" FT /id="VAR_051651" FT VARIANT 745 FT /note="K -> N" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040906" FT VARIANT 784..1258 FT /note="Missing (risk factor for ALS24)" FT /evidence="ECO:0000269|PubMed:26945885" FT /id="VAR_080696" FT VARIANT 883 FT /note="Q -> E (in dbSNP:rs6828134)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_046488" FT VARIANT 1008..1258 FT /note="Missing (risk factor for ALS24)" FT /evidence="ECO:0000269|PubMed:26945885" FT /id="VAR_080697" FT VARIANT 1180 FT /note="D -> N (in dbSNP:rs35503975)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_046489" FT CONFLICT 250 FT /note="N -> D (in Ref. 2; CAI45943)" FT /evidence="ECO:0000305" FT CONFLICT 602 FT /note="R -> RK (in Ref. 2; CAI45943)" FT /evidence="ECO:0000305" FT CONFLICT 1232 FT /note="G -> E (in Ref. 7; AAD42879)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 18..23 FT /evidence="ECO:0007829|PDB:4B9D" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 29..36 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 42..57 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 88..94 FT /evidence="ECO:0007829|PDB:4B9D" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 102..121 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4B9D" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 155..164 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 182..198 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 208..217 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 229..238 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 249..253 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 260..264 FT /evidence="ECO:0007829|PDB:4B9D" FT HELIX 268..275 FT /evidence="ECO:0007829|PDB:4B9D" SQ SEQUENCE 1258 AA; 142828 MW; 339C4BFA56612530 CRC64; MEKYVRLQKI GEGSFGKAIL VKSTEDGRQY VIKEINISRM SSKEREESRR EVAVLANMKH PNIVQYRESF EENGSLYIVM DYCEGGDLFK RINAQKGVLF QEDQILDWFV QICLALKHVH DRKILHRDIK SQNIFLTKDG TVQLGDFGIA RVLNSTVELA RTCIGTPYYL SPEICENKPY NNKSDIWALG CVLYELCTLK HAFEAGSMKN LVLKIISGSF PPVSLHYSYD LRSLVSQLFK RNPRDRPSVN SILEKGFIAK RIEKFLSPQL IAEEFCLKTF SKFGSQPIPA KRPASGQNSI SVMPAQKITK PAAKYGIPLA YKKYGDKKLH EKKPLQKHKQ AHQTPEKRVN TGEERRKISE EAARKRRLEF IEKEKKQKDQ IISLMKAEQM KRQEKERLER INRAREQGWR NVLSAGGSGE VKAPFLGSGG TIAPSSFSSR GQYEHYHAIF DQMQQQRAED NEAKWKREIY GRGLPERGIL PGVRPGFPYG AAGHHHFPDA DDIRKTLKRL KAVSKQANAN RQKGQLAVER AKQVEEFLQR KREAMQNKAR AEGHMVYLAR LRQIRLQNFN ERQQIKAKLR GEKKEANHSE GQEGSEEADM RRKKIESLKA HANARAAVLK EQLERKRKEA YEREKKVWEE HLVAKGVKSS DVSPPLGQHE TGGSPSKQQM RSVISVTSAL KEVGVDSSLT DTRETSEEMQ KTNNAISSKR EILRRLNENL KAQEDEKGKQ NLSDTFEINV HEDAKEHEKE KSVSSDRKKW EAGGQLVIPL DELTLDTSFS TTERHTVGEV IKLGPNGSPR RAWGKSPTDS VLKILGEAEL QLQTELLENT TIRSEISPEG EKYKPLITGE KKVQCISHEI NPSAIVDSPV ETKSPEFSEA SPQMSLKLEG NLEEPDDLET EILQEPSGTN KDESLPCTIT DVWISEEKET KETQSADRIT IQENEVSEDG VSSTVDQLSD IHIEPGTNDS QHSKCDVDKS VQPEPFFHKV VHSEHLNLVP QVQSVQCSPE ESFAFRSHSH LPPKNKNKNS LLIGLSTGLF DANNPKMLRT CSLPDLSKLF RTLMDVPTVG DVRQDNLEID EIEDENIKEG PSDSEDIVFE ETDTDLQELQ ASMEQLLREQ PGEEYSEEEE SVLKNSDVEP TANGTDVADE DDNPSSESAL NEEWHSDNSD GEIASECECD SVFNHLEELR LHLEQEMGFE KFFEVYEKIK AIHEDEDENI EICSKIVQNI LGNEHQHLYA KILHLVMADG AYQEDNDE //